title: Use of in vivo biotinylated GST fusion proteins to select recombinant antibodies.
abstract: Over the last 20 years, continuous advances in the field of molecular biology have led to the development of new strategies to discover and produce monoclonal antibodies, notably by phage display.Here we describe a simple procedure for antibody selection that reduces considerably the undesired selection of non-specific antibodies, based on the use of biotinylated GST proteins fused to a target antigenic sequence. This procedure was tested on a collection of 7 different targets and resulted in the selection of a high percentage (71%) of antibodies specific for each target. This simple and effective in vitro procedure has a strong potential to replace animal immunization for the development of specific antibodies.
authors.affiliation: Department of Cell Physiology and Metabolism, Centre Médical Universitaire, University of Geneva, 1 rue Michel Servet, CH1211, Geneva 4, Switzerland.
authors.forename: Cedric
authors.initials: C
authors.lastname: Blanc
authors.forename: Madeleine
authors.initials: M
authors.lastname: Zufferey
authors.forename: Pierre
authors.initials: P
authors.lastname: Cosson
mesh_terms: D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000737:chemistry*; D000941:Antigens; D019921:Biotinylation; D061505:Cell Surface Display Techniques; D005982:Glutathione Transferase / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000911:Antibodies, Monoclonal; D000941:Antigens; D011994:Recombinant Proteins; D005982:Glutathione Transferase